ID   CHS1_MUCCL              Reviewed;         852 AA.
AC   Q12632;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Chitin synthase 1;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
DE   AltName: Full=Class-II chitin synthase 1;
GN   Name=CHS1;
OS   Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=29924;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RA   Lopez-Matas A.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC       septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC       reducing end of the growing chitin polymer. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC         D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC         UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223; EC=2.4.1.16;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class II subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X99420; CAA67797.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12632; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; Q12632; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..852
FT                   /note="Chitin synthase 1"
FT                   /id="PRO_0000193713"
FT   TRANSMEM        492..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        572..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        601..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        787..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        830..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          27..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  95851 MW;  CB7CC0EB60FF8FA3 CRC64;
     MPSIKKQENS NAGGWFSSWF FSNTANEDQD DMLPSTSAAA GETNYARNQQ TLSSLRSQKS
     ANKPTTAQNR NSAATLVRTD TESYLDAPKS SRDQANGVLR RKVTRRLQLT NNNLVIDCPI
     PDRLLGALTF NDHDEFSQLR YTAATCEPDE FESRGFTLRP KIYNRETELF IVMTMYNEDE
     ILFTRTMHGV MKNIAHLCSL KKSTMWGPDG WKKVVVCIVA DGRQVVNKKV LDVLASMGVY
     QAGIAKNVVD DKPVKAHIYE YTTQISIDSD MNIKGSDKGI VPVQIMFCLK EKNAKKINSH
     RWFFNAFGPI IKPNVCILLD VGTRPGNSSI YQLWKVFDRN PLIGGACGEI RAMLGTACCQ
     LLNPLVAAQN FEYKMSNILD KPLESVFGYI SVLPGAFSAY RYAALKNDVN GHGPLEKYFI
     GEDLHSNLQG SSQSIKNTGL FEANMYLAED RILCFELVAK KDERWLLQYV GSAFGETDVP
     SQLPEFISQR RRWLNGSFFA GVYGLIHFRK IWNSGHGFNR TLLLMIEGIY NVISLVFSWF
     SVGNFYIAFY FITKSLSASN VDPFGNGWGS RIFDFCKYAY AFLLFVIFIC SMGNRPQGSK
     FLFMACLVGF AIIMCYMLFC SSWLIYKGIQ LAAEKYDWTY DTTTNFQIAM SDPGLRNMVI
     SLSSTYGIYL VSSCLHRQPF HMMTSFLPYL LLLPGYINIL NIYAFCNTHD VSWGTKGDNS
     VAKDLGVVKV SEKEKGVKTV EIELPADQHD INCQYDEALF ALDEKPSKDT GSGGSLTKDD
     YYRSFRTHLV LAWIACNALL VVFITTSDYE SIFNASVGTT YMSIMLWVNC GLGIFRFLGS
     IMFLLLGIFT SG